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CTSK  -  cathepsin K

Macaca mulatta

 
 
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Disease relevance of CTSK

 

High impact information on CTSK

  • It was shown that, unlike some peptidic nitrile inhibitors of cysteine proteases, the nitrile moiety of (R)-2 is not converted to the corresponding amide 3 by cathepsin K [1].
  • The P2-P3 amide bond of a known amino acetonitrile dipeptide 1 was replaced with a phenyl ring, thereby giving rise to this biaryl series that retained potency vs cathepsin K and showed an improved selectivity profile against other cathepsins [1].
  • Rhesus monkey cathepsin K was transiently expressed in Chinese hamster ovary (CHO) cells and found to be secreted as the proenzyme in the culture media and 50% activated to the mature form intracellularly [2].
  • Based on our previous study with trifluoroethylamine as a P2-P3 amide isostere of cathepsin K inhibitor, further optimization led to identification of compound 22 (L-873724) as a potent and selective non-basic cathepsin K inhibitor [3].
 

Chemical compound and disease context of CTSK

 

Analytical, diagnostic and therapeutic context of CTSK

References

  1. A novel class of nonpeptidic biaryl inhibitors of human cathepsin K. Robichaud, J., Oballa, R., Prasit, P., Falgueyret, J.P., Percival, M.D., Wesolowski, G., Rodan, S.B., Kimmel, D., Johnson, C., Bryant, C., Venkatraman, S., Setti, E., Mendonca, R., Palmer, J.T. J. Med. Chem. (2003) [Pubmed]
  2. Cloning and expression of rhesus monkey cathepsin K. Guay, J., Riendeau, D., Mancini, J.A. Bone (1999) [Pubmed]
  3. Identification of a potent and selective non-basic cathepsin K inhibitor. Li, C.S., Deschenes, D., Desmarais, S., Falgueyret, J.P., Gauthier, J.Y., Kimmel, D.B., Léger, S., Massé, F., McGrath, M.E., McKay, D.J., Percival, M.D., Riendeau, D., Rodan, S.B., Thérien, M., Truong, V.L., Wesolowski, G., Zamboni, R., Black, W.C. Bioorg. Med. Chem. Lett. (2006) [Pubmed]
 
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